8p7c

CryoEM structure of METTL6 tRNA SerRS complex in a 2:2:2 stoichiometry

Method: ELECTRON MICROSCOPY Dmax: 178.5 Å Quality: REASONABLE

1. Protein Identity and Related Structures Protein Identity & Related Structures

Serine--tRNA ligase, cytoplasmic

Homo sapiens

UniProt P49591

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain B; UniProt 1–514 Chain D; UniProt 1–514 Not recorded tRNA N(3)-methylcytidine methyltransferase METTL6 × 2 (Q8TCB7) Serine tRNA × 2 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

8 other PDB entries and 10 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name SYSC_HUMAN
Isoform
PDB entities 1
Chains and sequence ranges Author chain B; PDBConstruct 1–514; UniProt 1–514 Author chain D; PDBConstruct 1–514; UniProt 1–514

tRNA N(3)-methylcytidine methyltransferase METTL6

Homo sapiens

UniProt Q8TCB7

State in the Current Structure

Assembly Oligomeric State Construct Mutations and Modifications Ligands, Ions and Associated Components Method and Experimental Conditions Structure Quality
1 Protein–RNA Heteromer Protein × 4 RNA 2 PDB declaration: hexameric(6) Consistent with all polymer counts Chain A; UniProt 1–284 Chain C; UniProt 1–284 Not recorded Serine--tRNA ligase, cytoplasmic × 2 (P49591) Serine tRNA × 2 SAH S-ADENOSYL-L-HOMOCYSTEINE × 2 MG MAGNESIUM ION × 6 ELECTRON MICROSCOPY cryo-EM buffer:pH 7.5 cryo-EM vitrification conditions:Cryogen ETHANE Resolution 3.70 Å

Other States of the Same Protein in the Database

Each row is a biological assembly of the same UniProt protein in another PDB entry. The “Difference from current entry” column identifies evidence-level differences; no tag means the currently parsed fields agree.

6 other PDB entries and 9 assemblies. Open the comparison page and filter oligomeric states

View Construct and Data Evidence
UniProt name METL6_HUMAN
Isoform
PDB entities 2
Chains and sequence ranges Author chain A; PDBConstruct 1–284; UniProt 1–284 Author chain C; PDBConstruct 1–284; UniProt 1–284

The page prioritizes protein identity, the current assembly, associated components, oligomeric state and cross-PDB links. Chain mapping and sequence ranges are retained as data evidence. Internal IDs, import timestamps and assembly operation expressions are maintenance fields and are not shown here.

SAXS scattering curve SAXS Profile

SAXS profile for 8p7c

P(r) Distance Distribution P(r) Distribution

P(r) distribution for 8p7c
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2. Structure Basics 2. Structure Basics

Entry ID entry_id8p7c
Deposition date deposition_date2023-05-30
Structure title titleCryoEM structure of METTL6 tRNA SerRS complex in a 2:2:2 stoichiometry
Keywords keywordsMETTL6, tRNA, SerRS, Serine tRNA, 3-Methylcytosine, RNA BINDING PROTEIN; RNA BINDING PROTEIN
Experimental Method methodELECTRON MICROSCOPY

3. SAXS Parameters (CRYSOL theoretical calculation) 3. SAXS Parameters (CRYSOL)

Radius of gyration Rg (Guinier) rg_guinier48.20
Radius of gyration Rg (electron density) rg_electron49.76
Forward intensity I(0) i0864508000.00
Molecular weight molecular_weight205890.0 kDa
Excluded volume excluded_volume241870 ų
Envelope volume envelope_volume350160 ų
Hydration-shell volume shell_volume65255 ų
Envelope diameter envelope_diameter192.4
Shell Rg shell_rg46.79
Envelope Rg envelope_rg49.22
Shape Rg shape_rg49.81
Total Rg total_rg49.52
Total atoms total_atoms14273
Residues n_residues1503
Spherical-harmonic order n_harmonics20
q range q_range— – 0.5000 −1
Data points n_points101
Shell type shell_typedirectional
Solvent electron density solvent_density0.3340 e/ų
Shell contrast contrast_shell0.0300 e/ų
CRYSOL version crysol_version4.1.3

4. P(r) Distance Distribution (GNOM inversion) 4. P(r) Analysis (GNOM)

Maximum dimension Dmax dmax178.5
Rg (real space) rg_real51.37
Rg uncertainty (real space) rg_real_error1.12
I(0) (real space) i0_real8.7200e+08
I(0) uncertainty (real space) i0_real_error1.5890e+07
Rg (reciprocal space) rg_reciprocal48.21
I(0) (reciprocal space) i0_reciprocal863700000.0000
Solution quality estimate total_estimate0.6098
Solution quality rating solution_quality REASONABLE a REASONABLE solution
P(r) peaks n_peaks1
Primary peak position r_peak_primary48.7
Skewness Skewness skewness0.678
Kurtosis Kurtosis kurtosis-0.073
Angular range angular_range— – 0.1650 −1
Current regularization parameter α current_alpha1.2310
Highest regularization parameter α highest_alpha47220000.0000
Real-space data points n_real_points34
GNOM version gnom_version4.1.3
Quality Criteria quality_criteria AN1: 0.000; Oscil: 0.669; Stabil: 0.864; Sysdev: 0.000; Positv: 1.000; Valcen: 0.784; Smooth: 0.576

5. Crystallography and Experiment 5. Crystallography & Experiment

6. Entities and Polymers Entities & Polymers (6)

8. Citations (1)

9. Files and Curves (10)